2KK7
NMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii
Summary for 2KK7
| Entry DOI | 10.2210/pdb2kk7/pdb |
| NMR Information | BMRB: 16354 |
| Descriptor | V-type ATP synthase subunit E (1 entity in total) |
| Functional Keywords | subunit e, methanocaldococcus jannaschii, a1ao atp synthase, atp synthesis, hydrogen ion transport, ion transport, transport, hydrolase |
| Biological source | Methanocaldococcus jannaschii (Methanococcus jannaschii) |
| Total number of polymer chains | 1 |
| Total formula weight | 5767.81 |
| Authors | Gayen, S.,Balakrishna, A.,Gruber, G. (deposition date: 2009-06-16, release date: 2009-07-14, Last modification date: 2024-05-29) |
| Primary citation | Gayen, S.,Balakrishna, A.M.,Gruber, G. NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii J.Bioenerg.Biomembr., 41:343-348, 2009 Cited by PubMed Abstract: The N-termini of E and H of A1AO ATP synthase have been shown to interact and an NMR structure of N-terminal H1-47 has been solved recently. In order to understand the E-H assembly and the N-terminal structure of E, the truncated construct E1-52 of Methanocaldococcus jannaschii A1AO ATP synthase was produced, purified and the solution structure of E1-52 was determined by NMR spectroscopy. The protein is 60.5 A in length and forms an alpha helix between the residues 8-48. The molecule is amphipathic with a strip of hydrophobic residues, discussed as a possible helix-helix interaction with neighboring subunit H. PubMed: 19760172DOI: 10.1007/s10863-009-9237-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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